HDDA_CAMJE
ID HDDA_CAMJE Reviewed; 339 AA.
AC Q0P8I9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-glycero-alpha-D-manno-heptose 7-phosphate kinase {ECO:0000303|PubMed:31449400};
DE EC=2.7.1.168 {ECO:0000269|PubMed:31449400};
DE AltName: Full=D-alpha-D-heptose 7-phosphate kinase {ECO:0000305};
GN Name=hddA {ECO:0000312|EMBL:CAL35534.1};
GN OrderedLocusNames=Cj1425c {ECO:0000312|EMBL:CAL35534.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000312|EMBL:CAL35534.1};
RN [1] {ECO:0000312|EMBL:CAL35534.1, ECO:0000312|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000312|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:31449400};
RX PubMed=31449400; DOI=10.1021/acs.biochem.9b00548;
RA Huddleston J.P., Raushel F.M.;
RT "Biosynthesis of GDP-d-glycero-alpha-d-manno-heptose for the Capsular
RT Polysaccharide of Campylobacter jejuni.";
RL Biochemistry 58:3893-3902(2019).
RN [3] {ECO:0007744|PDB:4N3O}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000312|PDB:4N3O};
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Minasov G., Wawrzak Z., Gordon E., Onopriyenko O., Grimshaw S., Kwon K.,
RA Savchenko A., Anderson W.F.;
RT "2.4 Angstrom Resolution Crystal Structure of Putative Sugar Kinase from
RT Campylobacter jejuni.";
RL Submitted (OCT-2013) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-alpha-D-manno-
CC heptose 7-phosphate at the C-1 position to form D-glycero-alpha-D-
CC manno-heptose 1,7-bisphosphate. {ECO:0000269|PubMed:31449400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-alpha-D-manno-heptose 7-phosphate = ADP + D-
CC glycero-alpha-D-manno-heptose 1,7-bisphosphate + H(+);
CC Xref=Rhea:RHEA:27570, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60203, ChEBI:CHEBI:60207, ChEBI:CHEBI:456216;
CC EC=2.7.1.168; Evidence={ECO:0000269|PubMed:31449400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=103 uM for D-glycero-D-manno-heptose 7-phosphate (at pH 7.4 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31449400};
CC Note=kcat is 0.48 sec(-1) for D-glycero-D-manno-heptose 7-phosphate.
CC {ECO:0000269|PubMed:31449400};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-
CC heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-
CC glycero-alpha-D-manno-heptose 7-phosphate: step 1/3.
CC {ECO:0000269|PubMed:31449400}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:31449400}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35534.1; -; Genomic_DNA.
DR PIR; A81288; A81288.
DR RefSeq; WP_002858413.1; NC_002163.1.
DR RefSeq; YP_002344808.1; NC_002163.1.
DR PDB; 4N3O; X-ray; 2.40 A; A/B=1-339.
DR PDBsum; 4N3O; -.
DR AlphaFoldDB; Q0P8I9; -.
DR SMR; Q0P8I9; -.
DR STRING; 192222.Cj1425c; -.
DR PaxDb; Q0P8I9; -.
DR PRIDE; Q0P8I9; -.
DR EnsemblBacteria; CAL35534; CAL35534; Cj1425c.
DR GeneID; 905714; -.
DR KEGG; cje:Cj1425c; -.
DR PATRIC; fig|192222.6.peg.1406; -.
DR eggNOG; COG2605; Bacteria.
DR HOGENOM; CLU_048558_1_0_7; -.
DR OMA; LEIHHDG; -.
DR UniPathway; UPA00543; UER00606.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IC:UniProtKB.
DR GO; GO:2001060; P:D-glycero-D-manno-heptose 7-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR001174; Galkinase.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR014606; Heptose_7-P_kinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF036406; Hept_kin; 1.
DR PRINTS; PR00960; LMBPPROTEIN.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsule biogenesis/degradation;
KW Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="D-glycero-alpha-D-manno-heptose 7-phosphate kinase"
FT /id="PRO_0000454934"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT SITE 11
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT STRAND 3..18
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 28..47
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:4N3O"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4N3O"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:4N3O"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:4N3O"
SQ SEQUENCE 339 AA; 38142 MW; B004823F863776CC CRC64;
MKTIRTQTPL RLGLAGGGTD INLYCDKYTG YVLNATISLY IHCTLIKRED GKIIFDSPDT
NSYCEYESKE FLGNDGKLDI FKSIYNRIVK DFTKKPLSFS LHTYSDVPSG SGLGGSSTLV
VGVIKAFAEW LNLPLGEYEI AKLAYEIERE DLGIVGGAQD QYAATFGGFN FMEFYNNKRV
IVNPLRIKNW IASELEARTV LYFTNITREA KDIEEHKKGK LGDEKSLEAM HAIKQDAIKM
KEALFRADFG TLAQILGKSW RSKKIISEIV SNDELERIYK LAIDNGAYSG KTSGAGAGGF
MFFFVDPTKK YNLIKALRKE QGYVQDFSFT KEGVKSWRI
